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Literature summary for 1.4.1.1 extracted from

  • Crow, V.L.
    Properties of alanine dehydrogenase and aspartase from Propionibacterium freudenreichii subsp. shermanii (1987), Appl. Environ. Microbiol., 53, 1885-1892.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
NADH
-
Propionibacterium freudenreichii
NH4+
-
Propionibacterium freudenreichii
pyruvate inhibition at pH 7.5 greater than at pH 9.5; product inhibition Propionibacterium freudenreichii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-Ala + H2O + NAD+ Propionibacterium freudenreichii key enzyme in the metabolism of alanine, Ala is onyl fermented after lactate exhaustion and then at a slow rate pyruvate + NH3 + NADH
-
?

Organism

Organism UniProt Comment Textmining
Propionibacterium freudenreichii
-
subsp. shermanii
-

Purification (Commentary)

Purification (Comment) Organism
-
Propionibacterium freudenreichii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
17.1
-
-
Propionibacterium freudenreichii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala + H2O + NAD+
-
Propionibacterium freudenreichii pyruvate + NH3 + NADH
-
r
L-Ala + H2O + NAD+ key enzyme in the metabolism of alanine, Ala is onyl fermented after lactate exhaustion and then at a slow rate Propionibacterium freudenreichii pyruvate + NH3 + NADH
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.2 9.6
-
Propionibacterium freudenreichii

pH Range

pH Minimum pH Maximum Comment Organism
7 10.8 pH 7.0: 13% of maximal activity, pH 10.8: 52% of maximal activity Propionibacterium freudenreichii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Propionibacterium freudenreichii
NADH
-
Propionibacterium freudenreichii